2D 1H-31P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides.
The dynamics of hydration-water in several phospholipid membranes of different compositions is studied by 2D (1)H-(31)P heteronuclear correlation NMR under magic-angle spinning. By using a (1)H T(2) filter before and a (1)H mixing-time after the evolution period and (31)P detection, inter-bilayer water is selectively detected without resonance overlap from bulk water outside the multilamellar vesicles. Moreover the (1)H T(2) relaxation time of the inter-bilayer water is measured. Lipid membranes with labile protons either in the lipid headgroup or in sterols exhibit water-(31)P correlation peaks while membranes free of exchangeable protons do not, indicating that the mechanism for water-lipid correlation is chemical exchange followed by relayed magnetization transfer to (31)P. In the absence of membrane proteins, the inter-bilayer water (1)H T(2)'s are several tens of milliseconds. Incorporation of charged membrane peptides shortened this inter-bilayer water T(2) significantly. This T(2) reduction is attributed to the peptides' exchangeable protons, molecular motion and intermolecular hydrogen bonding, which affect the water dynamics and the chemically relayed magnetization transfer process.
Doherty
Tim
T
Department of Chemistry, Iowa State University, Ames, IA 50011, USA.
Hong
Mei
M
D008051:Lipid Bilayers / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D010759:Phosphorus Isotopes / Q000737:chemistry; D011522:Protons; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D008051:Lipid Bilayers; D008081:Liposomes; D008565:Membrane Proteins; D010743:Phospholipids; D010759:Phosphorus Isotopes; D011522:Protons; D014867:Water